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Q6TGQ8 (OXLA_BOTMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=BmooLAAO-I
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops moojeni (Lance-headed viper) (Caissaca)
Taxonomic identifier98334 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length478 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Phe>L-Tyr>L-Trp>L-Leu), thus producing hydrogen peroxide that may contribute to the toxicity of the venom. Exhibits diverse biological activities, such as edema, apoptosis of tumor cell lines, antibacterial activities against both Gram-positive and Gram-negative bacteria, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. It may also induce hemolysis, and have antiparasitic activities. Ref.2 Ref.3

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.2 Ref.3

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation. Ref.2

Miscellaneous

Has parasiticidal activities against and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.3, Ref.1).

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Mass spectrometry

Molecular mass is 64889 Da from positions 7 - ?. Determined by MALDI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 6›6 Ref.2
Chain7 – ›478›472L-amino-acid oxidase
PRO_0000273565

Regions

Nucleotide binding49 – 502FAD By similarity
Nucleotide binding69 – 702FAD By similarity
Nucleotide binding93 – 964FAD By similarity
Nucleotide binding470 – 4756FAD By similarity
Nucleotide binding470 – 4712Substrate By similarity

Sites

Binding site771FAD By similarity
Binding site961Substrate By similarity
Binding site2291Substrate By similarity
Binding site2671FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3781Substrate By similarity
Binding site4631FAD By similarity

Amino acid modifications

Glycosylation1781N-linked (GlcNAc...) Potential
Disulfide bond16 ↔ 179 By similarity
Disulfide bond337 ↔ 418 By similarity

Experimental info

Sequence conflict34 – 352ST → KS AA sequence Ref.2
Non-terminal residue11
Non-terminal residue4781

Sequences

Sequence LengthMass (Da)Tools
Q6TGQ8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 555C159B029FB9CB

FASTA47854,437
        10         20         30         40         50         60 
RKAPCCADDR NPLEECFRET DYEEFLEIAK NGLSTTSNPK RVVIVGAGMS GLSAAYVLAN 

        70         80         90        100        110        120 
AGHQVTVLEA SERAGGRVKT YRNEKEGWYA NLGPMRLPEK HRIVREYIRK FDLQLNEFSQ 

       130        140        150        160        170        180 
ENENAWYFIK NIRKRVGEVN KDPGVLEYPV KPSEVGKSAG QLYEESLQKA VEELRRTNCS 

       190        200        210        220        230        240 
YMLNKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFAYEKRFD 

       250        260        270        280        290        300 
EIVGGMDKLP TSMYQAIQEK VHLNARVIKI QQDVKEVTVT YQTSEKETLS VTADYVIVCT 

       310        320        330        340        350        360 
TSRAARRIKF EPPLPPKKAH ALRSVHYRSG TKIFLTCTKK FWEDDGIHGG KSTTDLPSRF 

       370        380        390        400        410        420 
IYYPNHNFPN GVGVIIAYGI GDDANYFQAL DFEDCGDIVI NDLSLIHQLP KEEIQAICRP 

       430        440        450        460        470 
SMIQRWSLDK YAMGGITTFT PYQFQHFSEA LTAPVDRIYF AGEYTAQAHG WIDSTIKW

« Hide

References

[1]"Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling."
Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V., Soares A.M.
Biochem. Biophys. Res. Commun. 355:302-306(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom and Venom gland.
[2]"Cytotoxic L-amino acid oxidase from Bothrops moojeni: biochemical and functional characterization."
Stabeli R.G., Sant'Ana C.D., Ribeiro P.H., Costa T.R., Ticli F.K., Pires M.G., Nomizo A., Albuquerque S., Malta-Neto N.R., Marins M., Sampaio S.V., Soares A.M.
Int. J. Biol. Macromol. 41:132-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 7-46, FUNCTION, SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY, CIRCULAR DICHROISM.
Tissue: Venom.
[3]"Bothrops moojeni venom kills Leishmania spp. with hydrogen peroxide generated by its L-amino acid oxidase."
Tempone A.G., Andrade H.F. Jr., Spencer P.J., Lourenco C.O., Rogero J.R., Nascimento N.
Biochem. Biophys. Res. Commun. 280:620-624(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY398692 mRNA. Translation: AAR31183.1.

3D structure databases

ProteinModelPortalQ6TGQ8.
SMRQ6TGQ8. Positions 9-477.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameOXLA_BOTMO
AccessionPrimary (citable) accession number: Q6TGQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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